Polyclonal Rabbit HSPA8 Antibody
- Known as:
- Polyclonal Rabbit HSPA8 Antibody
- Catalog number:
- KA1720
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit HSPA8 Antibody
Related genes to: Polyclonal Rabbit HSPA8 Antibody
- Gene:
- HSPA8 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 8
- Previous symbol:
- HSPA10
- Synonyms:
- HSC71, HSC70, HSP73
- Chromosome:
- 11q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-08
- Date modifiied:
- 2015-11-19
Related products to: Polyclonal Rabbit HSPA8 Antibody
Related articles to: Polyclonal Rabbit HSPA8 Antibody
- Glioma is a primary tumor derived from central nervous system glial cells. RNA binding motif protein 25 (RBM25) has been implicated in glioma progression, yet its underlying molecular mechanism remains incompletely understood. In this study, glioma-related datasets were retrieved from the Proteomic Data Commons (PDC) and Gene Expression Omnibus (GEO) databases. Core glioma-associated targets were screened using machine learning algorithms. Protein expression was assessed by Western blot, while migration, and invasion, cell cycle and apoptosis were analyzed by Transwell assay and flow cytometry. Chromatin immunoprecipitation (ChIP) and dual-luciferase reporter assays were used to validate the interaction between transcription factors and genes. Proteomic analysis revealed distinct differences between glioma and control groups, with differentially expressed proteins mainly enriched in mitochondrial energy metabolism, synaptic function, and neurodegenerative disease pathways. Transcriptomic profiles also exhibited significant alterations, with RBM25 and HSPA8 showing consistent changes at both protein and RNA levels. Multiple machine learning models identified RBM25, NKTR, MAP2K6, TRAPPC3, and HSPA8 as key genes associated with glioma, with RBM25 and NKTR showing strong relevance in model-based feature selection. RBM25 was upregulated in glioma and linked to neuronal signaling pathways, whereas HSPA8 and TRAPPC3 were downregulated. RBM25 knockdown suppressed glioma cell proliferation, migration, and invasion, and induced cell cycle arrest and apoptosis. In conclusion, RBM25 contributes to glioma malignancy and may serve as a potential biomarker and therapeutic target for glioma. - Source: PubMed
Publication date: 2026/05/29
Xu XiangdiWang JiahaoXue MingmingFeng Longkai - Bisphenol A (BPA) is a pervasive environmental endocrine disruptor implicated in hormone-related cancers.However, its association with non-hormone-dependent malignancies such as Diffuse Large B-cell Lymphoma (DLBCL) remains poorly understood.This study aimed to predict the potential molecular mechanisms linking BPA exposure to DLBCL pathogenesis through an integrated approach combining network toxicology and molecular docking.We systematically identified 46 overlapping genes shared between BPA-associated targets and DLBCL-related genes. Protein-protein interaction network analysis indicate six hub genes(HSP90AB1, HSPA8, CCNA2, CDK1, LDHA, and HSPA14),with HSP90AB1 exhibiting the highest topological centrality.Functional enrichment analysis demonstrated that these genes are significantly enriched in key oncogenic signaling pathways, including the PI3K-Akt and MAPK pathways, as well as critical biological processes such as protein folding and cell cycle regulation. Molecular docking simulations further predicted the stable binding affinity between BPA and each of the six hub proteins, with binding energies below - 6.0 kcal/mol. Collectively, our computational findings suggest a putative mechanistic framework in which BPA may contribute to DLBCL development by directly interacting with and potentially dysregulating central regulatory nodes in cellular networks, particularly the molecular chaperone HSP90AB1. These predictions require experimental validation but provide a basis for future mechanistic studies. - Source: PubMed
Publication date: 2026/05/27
Zhang YueJin Li - Coronavirus disease 2019 continues to pose global health challenges, with the pandemic significantly burdening several economies, healthcare systems, and the social lives of individuals. Furthermore, new cases continue to be reported, underscoring the need for therapeutic strategies targeting conserved regions and host-virus interactions. Building on earlier virtual screening for small molecules, all-atom molecular dynamics simulations and binding-free-energy calculations were performed to elucidate how the two previously identified small molecules (NSC36398 and NSC281245) may affect the dynamic behaviour of the interaction between heat shock 70 kDa protein 8 (HSPA8) and the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein. Post-MD analyses refined prior docking predictions, where NSC281245 was found to bind tightly to the complex with limited perturbations at the HSPA8-spike protein interaction surface, whereas NSC36398 appeared to induce allosteric-like domain-level destabilisation effects while maintaining stable polar contacts with the protein. Our findings demonstrate the potential of NSC36398 as a promising modulator for disrupting the HSPA8-spike protein complex, which may serve as a structural lead for designing next-generation inhibitors of host-virus interactions. - Source: PubMed
Publication date: 2026/05/12
Navhaya Liberty TMonama Mokgerwa ZMatsebatlela Thabe MMakhoba Xolani H - Protein-protein interactions (PPIs) play a central role in regulating cellular processes. However, the identification and characterization of senescence-associated PPIs remain challenging. In this study, we developed and evaluated an integrative methodology based on selective proteomics to identify PPIs associated with cellular senescence induced by TMPRSS11a. We started from isolated proteins that co-immunoprecipitated with TMPRSS11a and were subsequently identified by mass spectrometry. Building on this dataset, we implemented a workflow combining selective proteomics, structural bioinformatics, and experimental validation. Using this approach, we investigated the interaction between the transmembrane serine protease TMPRSS11a and the chaperone HSPA8. Structural bioinformatics analyses were performed to identify potential residues involved in the interaction interface, and the proximity of the TMPRSS11a-HSPA8 complex was evaluated using an in vitro proximity ligation assay. Our results provide evidence for an interaction between TMPRSS11a and HSPA8 and suggest its association with an enhanced senescence response. Overall, this study presents a workflow to investigate senescence-associated PPIs from proteomics-derived candidate proteins. - Source: PubMed
Publication date: 2026/05/13
Rosales-Rojas RobertoFernández ChristianGonzález-Avendaño MarielaVergara-Jaque ArielaCáceres Mónica - Fine particulate matter (PM) represents a pervasive global environmental hazard linked to adverse respiratory and systemic health outcomes, yet sensitive and noninvasive early biomarkers for real-world exposure remain poorly defined. In this 35 day panel study conducted in Shijiazhuang, China, we recruited 30 healthy young adult males to characterize proteomic and metabolomic alterations in exhaled breath condensate (EBC) under ambient PM exposure. The average personal PM concentration was 73.08 μg/m, with distinct high- and low-exposure periods of 131.33 and 40.46 μg/m, respectively. High PM exposure was associated with mild lung function decline, increased systemic inflammation, and elevated oxidative DNA damage. Proteomic profiling identified consistent downregulation of six key proteins in EBC, including PPIA, ENO1, EEF1A1, HSPA8, GAPDH, and RPSA. Metabolomic analysis further revealed disrupted energy metabolism and lipid homeostasis closely tied to inflammatory and oxidative stress responses. Notably, leucine, ornithine, and phenylalanine displayed consistent dose-response trends across EBC, plasma, and urine, supporting their promise as cross-compartment biomarkers. Our results validate EBC as a minimally invasive matrix to detect both local pulmonary and systemic perturbations induced by ambient PM exposure. - Source: PubMed
Publication date: 2026/05/20
Song QianOu ZehuaWang ZhitingLiu JianhuiYe LizhuJiang YueLiu WenjieZhang RuiWang ZiweiLi MiaoGuo YuzhiZhang JiahaoLi LianLi DaochuanZhang RongChen ShenZhang LihuaChen Wen